To enhance the adsorption performance of municipal sludge biochar on Cd(II), modified sludge biochar was prepared by sodium hydroxide/magnesium chloride (NaOH/MgCl2) graded activation, and the Cd(II) adsorption performance on sludge biochar (BC), NaOH-activated sludge biochar (NBC) and NaOH/MgCl2 activated sludge biochar (NBC-Mg) was investigated. The results showed that NaOH/MgCl2 graded activation upgraded the surface structure and enhanced the graphitization of sludge biochar. The adsorption experiments indicated that the adsorption kinetic and adsorption isotherm for Cd(II) were in accordance with the pseudo second-order kinetic and Langmuir model. The adsorption capacity of NBC-Mg (143.49 mg/g) for Cd(II) was higher than that of BC (50.40 mg/g) and NBC (85.20 mg/g). The mechanism of Cd(II) adsorption included ion exchange, complexation, cation-π interaction, and mineral precipitation. After five regeneration, the removal efficiency of Cd(II) by NBC-Mg remained above 90%. This work indicated that sludge biochar prepared by multistage activation could be an effective material for Cd-containing wastewater treatment.

Phosphorylation is an essential post-translational modification for regulating protein function and cellular signal transduction. Mass spectrometry (MS) combined with isobaric tandem mass tags (TMTs) has become a powerful platform for simultaneous, large-scale phospho-proteome site identification and quantitation. To improve the accuracy of isobaric tag-based quantitation in complex proteomic samples, MS3-based acquisition methods such as Synchronous Precursor Selection (SPS) have been used. However, the method suffers from lower peptide identification rates when applied to enriched phosphopeptide samples compared with unmodified samples due to differences in phosphopeptide fragmentation patterns during tandem MS. We developed and optimized two new acquisition methods for analysis of TMT-labeled multiplexed phosphoproteome samples, which resulted in more phosphopeptide identifications with less ratio distortion when compared with previous methods. We also applied these improved methods to a large-scale study of phosphorylation levels in A549 cell lines treated with insulin or insulin growth factor 1 (IGF-1). Overall, 3378 protein groups and 12 465 phosphopeptides were identified, of which 10 436 were quantified across 10 samples without prefractionation. The accurate measurement enabled us to map to numerous signaling pathways including mechanistic target of rapamycin (mTOR), epidermal growth factor receptor (EGFR, ErbB), and insulin signaling pathways.